Reviewed, UniProtKB/Swiss-Prot Q6TGQ8 (OXLA_BOTMO)

Names and origin

Protein names	Recommended name:     L-amino-acid oxidase       Short name=LAAO       Short name=LAO     EC=1.4.3.2
Organism	Bothrops moojeni (Lance-headed viper) (Caissaca)
Taxonomic identifier	98334 [NCBI]
Taxonomic lineage	Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Scleroglossa › Serpentes › Colubroidea › Viperidae › Crotalinae › Bothrops

Protein attributes

Sequence length	478 AA.
Sequence status	Fragment.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids. Inhibits platelet aggregation. Has an ability to induce apoptosis and hemorrhage. Has an antibacterial activity By similarity. Presents a killing effect in vitro against Leishmania spp promastigotes, but not with amastigotes.
Catalytic activity	An L-amino acid + H2O + O2 = a 2-oxo acid + NH3 + H2O2.
Cofactor	FAD By similarity.
Subunit structure	Homodimer. Ref.2
Subcellular location	Secreted By similarity.
Tissue specificity	Expressed by the venom gland.
Post-translational modification	Glycosylated By similarity.
Sequence similarities	Belongs to the flavin monoamine oxidase family. FIG1 subfamily.

Ontologies

Keywords
Biological process	Apoptosis Blood coagulation
Cellular component	Secreted
Domain	Signal
Ligand	FAD Flavoprotein
Molecular function	Antibiotic Antimicrobial Oxidoreductase Toxin
PTM	Disulfide bond Glycoprotein
Gene Ontology (GO)
Biological process	apoptosis Inferred from electronic annotation. Source: UniProtKB-KW blood coagulation Inferred from electronic annotation. Source: UniProtKB-KW defense response to bacterium Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW pathogenesis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	L-amino-acid oxidase activity Inferred from electronic annotation. Source: EC electron carrier activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	‹1 – 6	›6	By similarity
	Chain	7 – ›478	›472	L-amino-acid oxidase		PRO_0000273565
Regions
	Nucleotide binding	95 – 96	2	FAD By similarity
	Nucleotide binding	472 – 475	4	FAD By similarity
Sites
	Binding site	50	1	FAD By similarity
	Binding site	69	1	FAD By similarity
	Binding site	77	1	FAD By similarity
	Binding site	96	1	Substrate By similarity
	Binding site	229	1	Substrate By similarity
	Binding site	267	1	FAD; via amide nitrogen and carbonyl oxygen By similarity
	Binding site	378	1	Substrate By similarity
	Binding site	463	1	FAD By similarity
Amino acid modifications
	Glycosylation	178	1	N-linked (GlcNAc...) Potential
	Disulfide bond	16 ↔ 179		By similarity
	Disulfide bond	337 ↔ 418		By similarity
Experimental info
	Non-terminal residue	1	1
	Non-terminal residue	478	1

Sequences

	Sequence		Length	Mass (Da)
	Q6TGQ8-1 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: 555C159B029FB9CB	FASTA	478	54,437
	10 20 30 40 50 60 RKAPCCADDR NPLEECFRET DYEEFLEIAK NGLSTTSNPK RVVIVGAGMS GLSAAYVLAN 70 80 90 100 110 120 AGHQVTVLEA SERAGGRVKT YRNEKEGWYA NLGPMRLPEK HRIVREYIRK FDLQLNEFSQ 130 140 150 160 170 180 ENENAWYFIK NIRKRVGEVN KDPGVLEYPV KPSEVGKSAG QLYEESLQKA VEELRRTNCS 190 200 210 220 230 240 YMLNKYDTYS TKEYLLKEGN LSPGAVDMIG DLLNEDSGYY VSFIESLKHD DIFAYEKRFD 250 260 270 280 290 300 EIVGGMDKLP TSMYQAIQEK VHLNARVIKI QQDVKEVTVT YQTSEKETLS VTADYVIVCT 310 320 330 340 350 360 TSRAARRIKF EPPLPPKKAH ALRSVHYRSG TKIFLTCTKK FWEDDGIHGG KSTTDLPSRF 370 380 390 400 410 420 IYYPNHNFPN GVGVIIAYGI GDDANYFQAL DFEDCGDIVI NDLSLIHQLP KEEIQAICRP 430 440 450 460 470 SMIQRWSLDK YAMGGITTFT PYQFQHFSEA LTAPVDRIYF AGEYTAQAHG WIDSTIKW

References

[1]	"Structural and functional characterization of L-amino acid oxidase from Bothrops moojeni snake venom." Soares A.M., Kashima S., Roberto P.G., Astolfi-Filho S., Pereira J.O., Giglio J.R., Franca S.C. Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Venom gland.
[2]	"Bothrops moojeni venom kills Leishmania spp. with hydrogen peroxide generated by its L-amino acid oxidase." Tempone A.G., Andrade H.F. Jr., Spencer P.J., Lourenco C.O., Rogero J.R., Nascimento N. Biochem. Biophys. Res. Commun. 280:620-624(2001) [PubMed: 11162565] [Abstract] Cited for: FUNCTION, SUBUNIT. Tissue: Venom.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AY398692 mRNA. Translation: AAR31183.1.
3D structure databases
SMR	Q6TGQ8. Positions 10-477.
ModBase	Search...
Phylogenomic databases
HOVERGEN	Q6TGQ8.
Enzyme and pathway databases
BRENDA	1.4.3.2. 18617.
Family and domain databases
InterPro	IPR001613. Amineoxid_fl. IPR002937. Amino_oxidase. [Graphical view]
Pfam	PF01593. Amino_oxidase. 1 hit. [Graphical view]
PRINTS	PR00757. AMINEOXDASEF.
ProDom	PD000139. FAD_pyr_redox. 1 hit. [Graphical view] [Entries sharing at least one domain]
ProtoNet	Search...

Entry information

Entry name

OXLA_BOTMO

Accession

Primary (citable) accession number: Q6TGQ8

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 23, 2007
Last sequence update:	July 5, 2004
Last modified:	June 16, 2009
This is version 31 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Tox-Prot (Toxin Annotation Project)